Purification and Characterization of a New Lipase from Fusarium sp. YM-30
スポンサーリンク
概要
- 論文の詳細を見る
The extracellular lipase from Fusarium sp. YM-30 was purified by a procedure involving ultrafiltration, ammonium sulfate precipitation, and DEAE-Toyopearl 650M, CM-Toyopearl 650M, and Butyl-Toyopearl 650M column chromatographies. The purified lipase was homogeneous with 12kDa of molecular mass by SDS-PAGE, and had high specificities for mono- and di-acylglycerols, but low toward triacylglycerols. The enzyme had maximum activity at pH 7. 0 to 8. 0 and 37℃, and hydrolyzed digalactosyl diglyceride too.
- 社団法人日本農芸化学会の論文
- 1995-09-23
著者
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AKIBA Tetsunori
Research and Development Division, Amano Pharmaceutical Co., Ltd.
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MASE TAMIO
Research and Development Division, Amano Pharmaceutical Co. Ltd.,
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MATSUMIYA YUKO
Research and Development Division, Amano Pharmaceutical Co. Ltd.,
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Mase Tamio
Research And Development Division Amano Pharmaceutical Co. Ltd.
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Matsumiya Yuko
Research And Development Division Amano Pharmaceutical Co. Ltd.
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Akiba Tetsunori
Research And Development Division Amano Pharmaceutical Co. Ltd.
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